2361-97-9

Usage

Uses

Used in Neurological Health Supplements:
L-Phenylalanine, N-acetyl-, propyl ester is used as a cognitive enhancer for its ability to support the production of neurotransmitters such as dopamine, norepinephrine, and epinephrine. It is believed to have benefits for mood enhancement, memory and learning, and overall cognitive performance.
Used in Nootropic Formulas:
As a component of nootropic formulas, L-Phenylalanine, N-acetyl-, propyl ester is utilized for its potential to improve cognitive function and support brain health.
Used in Skincare Products:
L-Phenylalanine, N-acetyl-, propyl ester is used in skincare applications for its potential anti-aging and skin brightening effects, capitalizing on its antioxidant properties to protect the skin from oxidative stress and promote a youthful appearance.
Used in Antioxidant Therapies:
L-Phenylalanine, N-acetyl-, propyl ester is also considered for use in antioxidant therapies aimed at reducing oxidative stress in the brain, which may help in preventing or mitigating age-related cognitive decline.

Upstream product

• 71-23-8 propan-1-ol 
• 2018-61-3 (S)-2-acetylamino-3-phenylpropanoic acid 
• 67-56-1 methanol 
• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 14426-21-2 diethanolamine hydrochloride 
• 2901-75-9 (R,S)-N-acetyl phenylalanine 
• 4134-09-2 ethyl N-acetyl-DL-phenylalaninate 
• 3618-96-0 (S)-N-acetylphenylalanine 
• 173172-13-9 N-Acetyl-(D,L)-phenylalanine 2,2 2-trifluoroethyl ester 
• 108395-58-0 acetyl L-phenylalanine chloroethyl ester 

Relevant academic research and scientific papers

Ionic-surfactant-coated subtilisin: Activity, enantioselectivity, and application to dynamic kinetic resolution of secondary alcohols

In this work, we explored the utility of ionic-surfactant-coated Bacillus licheniformis subtilisin (ISCBLS) as the catalyst for the dynamic kinetic resolution of secondary alcohols. ISCBLS was prepared by freeze-drying Bacillus licheniformis subtilisin wi

NON-AQUEOUS ENZYME-POLYMER CONJUGATE SOLUTIONS AND RELATED METHODS

An enzyme-polymer conjugate shows increased activity and molecular dissolution in non-aqueous solvents enabling enzyme mediated catalysis in non-aqueous solutions. The inventions described in this specification relate to enzyme-polymer conjugates, organic

Urea treated subtilisin as a biocatalyst for transformations in organic solvents

Abstract Subtilisin lyophilized from its solution in aqueous buffer in the presence of 6 M urea showed up to 50-fold increase (as compared to lyophilized subtilisin not subjected to urea treatment) in its initial rate of a transesterification reaction in anhydrous n-hexane. The lyophilization time controlling the extent of 'drying' was an important parameter. The urea treated subtilisin had five times shorter half life during heating at 100 C in hexane. The change in conformation was also reflected in its 92-fold higher activity at 15 C as compared to merely 28-fold higher activity at 45 C. The comparative enantioselectivity of urea treated subtilisin during kinetic resolution of 1-phenylethanol was expectedly lower. Its enantioselectivity during kinetic resolution of a natural substrate N-acetyl-(R,S)-phenylalanine ethyl ester in hexane was higher. Urea treated subtilisin also showed higher catalytic promiscuity during an aldol condensation. CD studies in both far UV and near UV region were also carried out to compare the two structures.

Enhancing the catalytic efficiency of subtilisin for transesterification by dual bioimprinting

Bioimprinting is a technique in which an aqueous solution of a protein molecule along with the imprint molecule is dried to remove bulk water. Subtilisin was dissolved in an aqueous buffer with a substrate analog and precipitated with the substrate alcoho

Protease activation in glycerol-based deep eutectic solvents

Deep eutectic solvents (DESs) consisting of mixtures of a choline salt (chloride or acetate form) and glycerol are prepared as easily accessible, biodegradable, and inexpensive alternatives to conventional aprotic cation-anion paired ionic liquids. These DES systems display excellent fluidity coupled with thermal stability to nearly 200 °C. In this work, the transesterification activities of cross-linked proteases (subtilisin and α-chymotrypsin), immobilized on chitosan, were individually examined in these novel DESs. In the 1:2 molar ratio mixture of choline chloride/glycerol containing 3% (v/v) water, cross-linked subtilisin exhibited an excellent activity (2.9 μmol min -1 g-1) in conjunction with a selectivity of 98% in the transesterification reaction of N-acetyl-l-phenylalanine ethyl ester with 1-propanol. These highly encouraging results advocate more extensive exploration of DESs in protease-mediated biotransformations of additional polar substrates and use of DESs in biocatalysis more generally.

Soluble, folded and active subtilisin in a protic ionic liquid

The activity of proteases chymotrypsin and subtilisin dissolved in a range of protic hydroxylalkylammonium ionic liquids was tested against the model substrate APEE (N-acetyl-l-phenylalanine ethyl ester); activity was only observed for subtilisin in diethanolammonium chloride (DEA Cl), while chymotrypsin was not active in any PIL tested.

Active-site motions and polarity enhance catalytic turnover of hydrated subtilisin dissolved in organic solvents

The enzyme subtilisin Carlsberg was surfactant-solubilized into two organic solvents, isooctane and tetrahydrofuran, and hydrated through stepwise changes in the thermodynamic water activity, aw. The apparent turnover number Acatsup

Enhanced activity of α-chymotrypsin in organic media using designed molecular staples

We report the enhancement of α-chymotrypsin activity in organic solvents using modified peptides bearing two crown ethers. The transesterification of N-acetyl-l-phenylalanine ethyl ester with 1-propanol was used as model reaction. Co-lyophilization of cro

Nanophase separated amphiphilic microbeads

The synthesis of nonporous nanophase separated amphiphilic microbeads was investigated. The synthesis was performed with a mixture of α,ω- methacrylate-terminated poly-dimethylsiloxane (MA-PDMS-MA), trimethylsilylated 2-hydroxyethylacrylate (TMSOEA) and t

Fluorometric Assay Protocol for Protease-Catalyzed Transesterification Reactions in Organic Solvents

A flourometric assay protocol for a subtilisin-catalyzed transesterification reaction in n-hexane has been developed. The method makes use of a Michael acceptor that forms a fluorescent adduct with thiophenol, one of the products generated in the transest